Sunghoon Kim's Aminoacyl-tRNA Synthetases in Biology and Medicine PDF

By Sunghoon Kim

ISBN-10: 940178700X

ISBN-13: 9789401787000

ISBN-10: 9401787018

ISBN-13: 9789401787017

This publication will specialize in new molecular interactions and novel actions and the linked ailments which have been lately stumbled on from the stories of eukaryotic and mammalian aminoacyl-tRNA synthetases. moreover, the capability purposes of ARS researches in biotechnology and drugs can be addressed.

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Additional resources for Aminoacyl-tRNA Synthetases in Biology and Medicine

Sample text

Several surface loops shown in magenta also become ordered when tRNA binds in the synthetic site proteins that correspond to a number of class II editing domains but not to the common CP1 editing domain of class I aaRS (see below). Details of the substrate specificity and catalytic mechanisms in the editing domains are emerging from crystal structures and mutational analysis [2]. Atomic level depictions of the active sites, including the solvent structure, have been provided by high resolution structures of separately expressed editing domains and homologous free-standing proteins (see below) [154, 196–203].

Synthetic and Editing Mechanisms of Aminoacyl-tRNA Synthetases 25 The three class I enzymes that catalyze post-transfer editing each possess a common mixed α/β domain (CP1) inserted into the Rossmann fold (Fig. 1, Table 1) [27]. In mitochondrial and bacterial LeuRS, the precise position of CP1 insertion differs as compared with IleRS, ValRS, and archaeal/eukaryotic LeuRS, but the ˚ spatial separation of the synthetic and editing active sites is approximately 30–40 A in all the enzymes [78, 152, 153, 193].

Bullock TL, Uter N, Nissan TA, Perona JJ (2003) Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified by negative determinants. J Mol Biol 328:395–408 74. Corigliano EM, Perona JJ (2009) Architectural underpinnings of the genetic code for glutamine. Biochemistry 48:676–687 75. Konno M, Sumida T, Uchikawa E, Mori Y, Yanagisawa T, Sekine S, Yokoyama S (2009) Modeling of tRNA-assisted mechanism of Arg activation based on a structure of Arg-tRNA synthetase, tRNA, and an ATP analog (ANP).

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Aminoacyl-tRNA Synthetases in Biology and Medicine by Sunghoon Kim


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